Escherichia coli RNase E can efficiently replace RNase Y in Bacillus subtilis.

Soumaya Laalami, Marina Cavaiuolo, Sylvain Roque, Carine Chagneau, Harald Putzer

Nucleic acids research 2021 May 07

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RNase Y and RNase E are disparate endoribonucleases that govern global mRNA turnover/processing in the two evolutionary distant bacteria Bacillus subtilis and Escherichia coli, respectively. The two enzymes share a similar in vitro cleavage specificity and subcellular localization. To evaluate the potential equivalence in biological function between the two enzymes in vivo we analyzed whether and to what extent RNase E is able to replace RNase Y in B. subtilis. Full-length RNase E almost completely restores wild type growth of the rny mutant. This is matched by a surprising reversal of transcript profiles both of individual genes and on a genome-wide scale. The single most important parameter to efficient complementation is the requirement for RNase E to localize to the inner membrane while truncation of the C-terminal sequences corresponding to the degradosome scaffold has only a minor effect. We also compared the in vitro cleavage activity for the major decay initiating ribonucleases Y, E and J and show that no conclusions can be drawn with respect to their activity in vivo. Our data confirm the notion that RNase Y and RNase E have evolved through convergent evolution towards a low specificity endonuclease activity universally important in bacteria. © The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

Citation

Soumaya Laalami, Marina Cavaiuolo, Sylvain Roque, Carine Chagneau, Harald Putzer. Escherichia coli RNase E can efficiently replace RNase Y in Bacillus subtilis. Nucleic acids research. 2021 May 07;49(8):4643-4654